Structure of severin domain 2 in solution.

@article{Schnuchel1995StructureOS,
  title={Structure of severin domain 2 in solution.},
  author={Arndt Schnuchel and Ronald Wiltscheck and Ludwig Eichinger and Michael Schleicher and Tad A. Holak},
  journal={Journal of molecular biology},
  year={1995},
  volume={247 1},
  pages={21-7}
}
The three-dimensional structure of domain 2 of severin in aqueous solution was determined by nuclear magnetic resonance spectroscopy. Severin is a Ca(2+)-activated actin-binding protein that servers F-actin, nucleates actin assembly, and caps the fast-growing ends of actin filaments. The 114-residue domain consists of a central five-stranded beta-sheet, sandwiched between a parallel four-turn alpha-helix and, on the other face, a roughly perpendicular two-turn alpha-helix. There are two… CONTINUE READING

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